2025
RNA N-glycosylation enables immune evasion and homeostatic efferocytosis
Graziano V, Porat J, Ah Kioon M, Mejdrová I, Matz A, Lebedenko C, Chai P, Pluvinage J, Ricci-Azevedo R, Harrison A, Wright S, Wang X, Strine M, Wang P, Wilson M, Vanaja S, Zhou B, Barrat F, Carell T, Flynn R, Rathinam V. RNA N-glycosylation enables immune evasion and homeostatic efferocytosis. Nature 2025, 645: 784-792. PMID: 40770106, DOI: 10.1038/s41586-025-09310-6.Peer-Reviewed Original ResearchConceptsNon-inflammatory clearanceN-glycansSmall RNAsInnate immune sensingApoptotic cellsEndogenous small RNAsFunctional significanceProduction of type I interferonsDe-N-glycosylationInnate immune activationEndosomal networkInnate immune responseClearance of dead cellsN-glycosylationRNA sensorsType I interferonToll-like receptorsRNAGlycoRNACell surfaceGenetic deletionI interferonDead cellsAcp3UAutoinflammatory responses
2024
Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis
Parolek J, Burd C. Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis. Molecular Biology Of The Cell 2024, 35: br11. PMID: 38536441, PMCID: PMC11151097, DOI: 10.1091/mbc.e24-02-0065.Peer-Reviewed Original ResearchConceptsLipid transfer proteinsFamily member 2RPE-1 cellsSuppressed ciliogenesisTubular endosomal networkMembrane contact sitesNegative regulator of ciliogenesisRegulator of ciliogenesisDrosophila melanogaster</i>Evolutionary conserved proteinMember 2Primary cilium biogenesisRPE-1Endosomal networkGenetic interactionsTubular endosomesCilium biogenesisProtein familyStructure predictionContact sitesEndoplasmic reticulumDomain-containingPreweaning lethalityNegative regulatorCiliogenesis
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